ID M1VL97_CYAM1 Unreviewed; 449 AA.
AC M1VL97;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Protein-serine/threonine kinase {ECO:0000256|RuleBase:RU366032};
DE EC=2.7.11.- {ECO:0000256|RuleBase:RU366032};
GN ORFNames=CYME_CMR225C {ECO:0000313|EMBL:BAM82458.1};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699 {ECO:0000313|EMBL:BAM82458.1, ECO:0000313|Proteomes:UP000007014};
RN [1] {ECO:0000313|EMBL:BAM82458.1, ECO:0000313|Proteomes:UP000007014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10D {ECO:0000313|EMBL:BAM82458.1,
RC ECO:0000313|Proteomes:UP000007014};
RX PubMed=15071595; DOI=10.1038/nature02398;
RA Matsuzaki M., Misumi O., Shin-i T., Maruyama S., Takahara M.,
RA Miyagishima S., Mori T., Nishida K., Yagisawa F., Nishida K., Yoshida Y.,
RA Nishimura Y., Nakao S., Kobayashi T., Momoyama Y., Higashiyama T.,
RA Minoda A., Sano M., Nomoto H., Oishi K., Hayashi H., Ohta F., Nishizaka S.,
RA Haga S., Miura S., Morishita T., Kabeya Y., Terasawa K., Suzuki Y.,
RA Ishii Y., Asakawa S., Takano H., Ohta N., Kuroiwa H., Tanaka K.,
RA Shimizu N., Sugano S., Sato N., Nozaki H., Ogasawara N., Kohara Y.,
RA Kuroiwa T.;
RT "Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon
RT merolae 10D.";
RL Nature 428:653-657(2004).
RN [2] {ECO:0000313|EMBL:BAM82458.1, ECO:0000313|Proteomes:UP000007014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10D {ECO:0000313|EMBL:BAM82458.1,
RC ECO:0000313|Proteomes:UP000007014};
RX PubMed=17623057; DOI=10.1186/1741-7007-5-28;
RA Nozaki H., Takano H., Misumi O., Terasawa K., Matsuzaki M., Maruyama S.,
RA Nishida K., Yagisawa F., Yoshida Y., Fujiwara T., Takio S., Tamura K.,
RA Chung S.J., Nakamura S., Kuroiwa H., Tanaka K., Sato N., Kuroiwa T.;
RT "A 100%-complete sequence reveals unusually simple genomic features in the
RT hot-spring red alga Cyanidioschyzon merolae.";
RL BMC Biol. 5:28-28(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP
CC + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit];
CC Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036431};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU366032}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000256|ARBA:ARBA00006155, ECO:0000256|RuleBase:RU366032}.
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DR EMBL; AP006500; BAM82458.1; -; Genomic_DNA.
DR RefSeq; XP_005538494.1; XM_005538437.1.
DR AlphaFoldDB; M1VL97; -.
DR STRING; 280699.M1VL97; -.
DR EnsemblPlants; CMR225CT; CMR225CT; CMR225C.
DR GeneID; 16996755; -.
DR Gramene; CMR225CT; CMR225CT; CMR225C.
DR KEGG; cme:CYME_CMR225C; -.
DR eggNOG; KOG0787; Eukaryota.
DR HOGENOM; CLU_023861_5_1_1; -.
DR OMA; NEMPSIC; -.
DR OrthoDB; 3058550at2759; -.
DR Proteomes; UP000007014; Chromosome 18.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16929; HATPase_PDK-like; 1.
DR Gene3D; 1.20.140.20; Alpha-ketoacid/pyruvate dehydrogenase kinase, N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR039028; BCKD/PDK.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR PANTHER; PTHR11947:SF3; [PYRUVATE DEHYDROGENASE (ACETYL-TRANSFERRING)] KINASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11947; PYRUVATE DEHYDROGENASE KINASE; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF69012; alpha-ketoacid dehydrogenase kinase, N-terminal domain; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366032};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU366032};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU366032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366032}; Pyruvate {ECO:0000313|EMBL:BAM82458.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007014};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366032}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..449
FT /note="Protein-serine/threonine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004018580"
FT DOMAIN 306..442
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 449 AA; 50104 MW; 040C30638CCD818E CRC64;
MAIWRKQGLA WAVLRLGSGL WPSATRGWTS AQRLAPAASL RTSAEDPSIP SWLASGCPPS
QPDVAYTPLE AKPLLLRLPS SREEALELIP RYARRSATPV SLRQLLEFGR HPTPKKLLLA
AQLMHRELAI RLAHRVVELQ SLPYGLSEMR SVKRVCELYE NSFADILMHP RPEREGEEER
RFTELLRRIR DRHSDVVRQI ACGVLELKQS CGMGADDIHI SSFLDRFYTS RIGIRVLISQ
QVSMSLERSR QGYVGIIHIR CRPAHVAADA ADAARALAYR HYGEEPPEVV ILGKTDLEFP
YIEGHLYHVL FELLKNSIRA TMEHHMGRES FPPIKVIIAD GYEDVTLKIA DEGGGISRSS
LPKIWTYMFT TATVPPEALI QPEYGPGSHV HGARGASMDP LAGFGYGLPL SRLYARYFGG
ELSIASMEGF GTDAYVHLAK LGNRLEALV
//
